ID B9J0Q2_BACCQ Unreviewed; 397 AA.
AC B9J0Q2;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Thermitase {ECO:0000313|EMBL:ACM12734.1};
GN OrderedLocusNames=BCQ_2306 {ECO:0000313|EMBL:ACM12734.1};
OS Bacillus cereus (strain Q1).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=361100 {ECO:0000313|EMBL:ACM12734.1, ECO:0000313|Proteomes:UP000000441};
RN [1] {ECO:0000313|EMBL:ACM12734.1, ECO:0000313|Proteomes:UP000000441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Q1 {ECO:0000313|EMBL:ACM12734.1,
RC ECO:0000313|Proteomes:UP000000441};
RX PubMed=19060151; DOI=10.1128/JB.01629-08;
RA Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X.,
RA Xue Y., Zhu Y., Jin Q.;
RT "Complete genome sequence of the extremophilic Bacillus cereus strain Q1
RT with industrial applications.";
RL J. Bacteriol. 191:1120-1121(2009).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000227; ACM12734.1; -; Genomic_DNA.
DR AlphaFoldDB; B9J0Q2; -.
DR SMR; B9J0Q2; -.
DR KEGG; bcq:BCQ_2306; -.
DR HOGENOM; CLU_011263_15_6_9; -.
DR Proteomes; UP000000441; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07484; Peptidases_S8_Thermitase_like; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034084; Thermitase-like_dom.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 139..367
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 146
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 179
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 333
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 397 AA; 42346 MW; 03CA22FA3DA63BF1 CRC64;
MKNKIIVFLS VLSFIIGGFF FNTNTSSAET SSTDYVPNQL IVKFKQNASL SNVQSFHKSV
GANVLSKDDK LGFEVVQFSK GTVKEKIKSY KNNPDVEYAE PNYYVHAFWT PNDPYFKNQY
GLQKIQAPQA WDSQRSDPGV KVAIIDTGVQ GSHPDLASKV IYGHDYVDND NTSDDGNGHG
THCAGITGAL TNNSVGIAGV APQTSIYAVR VLDNQGSGTL DAVAQGIREA ADSGAKVISL
SLGAPNGGTA LQQAVQYAWN KGSVIVAAAG NAGNTKANYP AYYSEVIAVA STDQLDKKSS
FSTYGSWVDV AAPGSNIYST YKGSTYQSLS GTSMATPHVA GVAALLANQG YSNTQIRQII
ESTSDKITGT GTYWKNGRVN AYKAVQYAKQ LQENKAS
//
